HEADER TRANSPORT PROTEIN 03-SEP-12 4GX1
TITLE CRYSTAL STRUCTURE OF THE GSUK BOUND TO ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRKA DOMAIN PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACTER SULFURREDUCENS;
SOURCE 3 ORGANISM_TAXID: 243231;
SOURCE 4 STRAIN: ATCC 51573 / DSM 12127 / PCA;
SOURCE 5 GENE: GSU0527;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE-70
KEYWDS MEMBRANE PROTEIN, ION CHANNEL, ADP BINDING, NAD BINDING, MEMBRANE,
KEYWDS 2 TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.KONG,W.ZENG,S.YE,L.CHEN,D.B.SAUER,Y.LAM,M.G.DEREBE,Y.JIANG
REVDAT 3 28-FEB-24 4GX1 1 HETSYN
REVDAT 2 29-JUL-20 4GX1 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 2 1 LINK SITE
REVDAT 1 26-DEC-12 4GX1 0
JRNL AUTH C.KONG,W.ZENG,S.YE,L.CHEN,D.B.SAUER,Y.LAM,M.G.DEREBE,Y.JIANG
JRNL TITL DISTINCT GATING MECHANISMS REVEALED BY THE STRUCTURES OF A
JRNL TITL 2 MULTI-LIGAND GATED K(+) CHANNEL.
JRNL REF ELIFE V. 1 00184 2012
JRNL REFN ESSN 2050-084X
JRNL PMID 23240087
JRNL DOI 10.7554/ELIFE.00184
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 71566
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 3623
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.4743 - 8.2740 0.90 2524 148 0.2295 0.2362
REMARK 3 2 8.2740 - 6.5758 0.94 2552 147 0.2013 0.2289
REMARK 3 3 6.5758 - 5.7470 0.95 2614 127 0.2323 0.2628
REMARK 3 4 5.7470 - 5.2227 0.95 2571 124 0.2160 0.2757
REMARK 3 5 5.2227 - 4.8489 0.96 2593 132 0.1614 0.2255
REMARK 3 6 4.8489 - 4.5634 0.96 2625 151 0.1532 0.1760
REMARK 3 7 4.5634 - 4.3351 0.96 2573 140 0.1535 0.2122
REMARK 3 8 4.3351 - 4.1466 0.97 2595 150 0.1668 0.2027
REMARK 3 9 4.1466 - 3.9871 0.97 2636 123 0.1834 0.2042
REMARK 3 10 3.9871 - 3.8496 0.97 2610 142 0.1906 0.2739
REMARK 3 11 3.8496 - 3.7293 0.97 2651 139 0.1942 0.2532
REMARK 3 12 3.7293 - 3.6228 0.97 2595 158 0.2219 0.2620
REMARK 3 13 3.6228 - 3.5275 0.98 2636 122 0.2137 0.2488
REMARK 3 14 3.5275 - 3.4415 0.98 2645 134 0.2153 0.2948
REMARK 3 15 3.4415 - 3.3633 0.97 2613 148 0.2191 0.2867
REMARK 3 16 3.3633 - 3.2917 0.98 2614 144 0.2350 0.2970
REMARK 3 17 3.2917 - 3.2259 0.98 2640 142 0.2484 0.3189
REMARK 3 18 3.2259 - 3.1650 0.98 2643 124 0.2648 0.3181
REMARK 3 19 3.1650 - 3.1085 0.98 2630 140 0.2661 0.3097
REMARK 3 20 3.1085 - 3.0559 0.98 2677 146 0.2663 0.3196
REMARK 3 21 3.0559 - 3.0066 0.98 2572 154 0.2736 0.3756
REMARK 3 22 3.0066 - 2.9603 0.98 2648 147 0.3000 0.3155
REMARK 3 23 2.9603 - 2.9168 0.98 2656 132 0.3048 0.3586
REMARK 3 24 2.9168 - 2.8757 0.98 2588 160 0.3151 0.4153
REMARK 3 25 2.8757 - 2.8369 0.98 2695 119 0.3280 0.3859
REMARK 3 26 2.8369 - 2.8000 0.96 2547 130 0.3277 0.3559
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.73
REMARK 3 K_SOL : 0.27
REMARK 3 B_SOL : 47.85
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.480
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.17900
REMARK 3 B22 (A**2) : -14.24430
REMARK 3 B33 (A**2) : 10.06530
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.00300
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 14702
REMARK 3 ANGLE : 0.902 20046
REMARK 3 CHIRALITY : 0.063 2401
REMARK 3 PLANARITY : 0.004 2535
REMARK 3 DIHEDRAL : 16.817 5402
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 18:118 ) OR ( CHAIN B AND RESID
REMARK 3 18:118 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6903 48.7894 9.2215
REMARK 3 T TENSOR
REMARK 3 T11: 0.5228 T22: 0.3708
REMARK 3 T33: 0.6489 T12: 0.0424
REMARK 3 T13: -0.0751 T23: 0.0765
REMARK 3 L TENSOR
REMARK 3 L11: 2.1158 L22: 1.5880
REMARK 3 L33: 2.0274 L12: 0.3610
REMARK 3 L13: -0.4285 L23: 0.3082
REMARK 3 S TENSOR
REMARK 3 S11: -0.0238 S12: -0.1128 S13: -0.1932
REMARK 3 S21: 0.4184 S22: 0.1330 S23: -0.1057
REMARK 3 S31: 0.3649 S32: -0.0234 S33: -0.0922
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN C AND RESID 19:118 ) OR ( CHAIN D AND RESID
REMARK 3 18:118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -56.0564 20.8719 67.6330
REMARK 3 T TENSOR
REMARK 3 T11: 0.7194 T22: 0.3659
REMARK 3 T33: 0.4918 T12: 0.0176
REMARK 3 T13: -0.0224 T23: 0.0626
REMARK 3 L TENSOR
REMARK 3 L11: 2.0764 L22: 1.9569
REMARK 3 L33: 1.5649 L12: -0.7832
REMARK 3 L13: -0.1838 L23: 0.7620
REMARK 3 S TENSOR
REMARK 3 S11: -0.0569 S12: -0.2071 S13: -0.2723
REMARK 3 S21: 0.5470 S22: 0.0662 S23: 0.1351
REMARK 3 S31: 0.2652 S32: -0.0640 S33: -0.0418
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND ( RESID 119:261 OR RESID 350:481 OR
REMARK 3 RESID 604:604 OR RESID 606:606 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0118 -12.9470 25.8048
REMARK 3 T TENSOR
REMARK 3 T11: 0.3723 T22: 0.3385
REMARK 3 T33: 0.2380 T12: 0.0276
REMARK 3 T13: -0.0574 T23: -0.0569
REMARK 3 L TENSOR
REMARK 3 L11: 6.9587 L22: 2.1159
REMARK 3 L33: 0.6133 L12: 3.0777
REMARK 3 L13: -1.1267 L23: -0.4095
REMARK 3 S TENSOR
REMARK 3 S11: 0.1329 S12: -0.0944 S13: 0.0909
REMARK 3 S21: 0.1725 S22: 0.0159 S23: -0.0116
REMARK 3 S31: 0.0760 S32: -0.0093 S33: -0.1402
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN B AND ( RESID 119:260 OR RESID 350:480 OR
REMARK 3 RESID 604:604 OR RESID 606:606 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7555 -12.5194 2.4619
REMARK 3 T TENSOR
REMARK 3 T11: 0.3000 T22: 0.3814
REMARK 3 T33: 0.6605 T12: 0.0487
REMARK 3 T13: 0.0892 T23: 0.1398
REMARK 3 L TENSOR
REMARK 3 L11: 0.6783 L22: 1.4125
REMARK 3 L33: 6.9262 L12: 0.2929
REMARK 3 L13: 1.5736 L23: 1.9116
REMARK 3 S TENSOR
REMARK 3 S11: -0.0272 S12: -0.0444 S13: 0.0526
REMARK 3 S21: -0.0093 S22: 0.0736 S23: 0.0671
REMARK 3 S31: -0.3219 S32: -0.0101 S33: 0.0118
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN C AND ( RESID 119:261 OR RESID 351:482 OR
REMARK 3 RESID 604:604 OR RESID 607:607 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.1110 -40.6379 83.6597
REMARK 3 T TENSOR
REMARK 3 T11: 0.5723 T22: 0.3317
REMARK 3 T33: 0.3505 T12: 0.1201
REMARK 3 T13: -0.0735 T23: -0.0858
REMARK 3 L TENSOR
REMARK 3 L11: 6.3508 L22: 0.8228
REMARK 3 L33: 0.9049 L12: 1.3661
REMARK 3 L13: -1.2910 L23: -0.5287
REMARK 3 S TENSOR
REMARK 3 S11: -0.0415 S12: 0.1186 S13: 0.1787
REMARK 3 S21: 0.1515 S22: -0.0258 S23: 0.0106
REMARK 3 S31: -0.1608 S32: -0.0159 S33: 0.0596
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN D AND ( RESID 119:261 OR RESID 351:482 OR
REMARK 3 RESID 603:603 OR RESID 604:604 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -83.8747 -40.7175 59.1903
REMARK 3 T TENSOR
REMARK 3 T11: 0.2522 T22: 0.3786
REMARK 3 T33: 0.4594 T12: 0.0380
REMARK 3 T13: 0.0409 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.7498 L22: 2.3245
REMARK 3 L33: 7.3893 L12: 0.2320
REMARK 3 L13: 0.8059 L23: 3.1189
REMARK 3 S TENSOR
REMARK 3 S11: -0.0378 S12: -0.0125 S13: 0.0340
REMARK 3 S21: -0.0205 S22: 0.0172 S23: 0.1774
REMARK 3 S31: -0.1171 S32: -0.0687 S33: 0.0275
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN B AND ( RESID 261:349 OR RESID 481:564 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -54.0499 -13.3475 5.6674
REMARK 3 T TENSOR
REMARK 3 T11: 0.6788 T22: 0.8028
REMARK 3 T33: 1.0114 T12: 0.0465
REMARK 3 T13: 0.0981 T23: 0.1509
REMARK 3 L TENSOR
REMARK 3 L11: 5.3742 L22: 7.4270
REMARK 3 L33: 5.0477 L12: -2.4579
REMARK 3 L13: -1.2516 L23: 1.4164
REMARK 3 S TENSOR
REMARK 3 S11: -0.2406 S12: -0.5076 S13: 0.0803
REMARK 3 S21: 1.3501 S22: 0.1007 S23: 1.0432
REMARK 3 S31: -0.3190 S32: -0.6152 S33: 0.1184
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN C AND ( RESID 262:350 OR RESID 483:564 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -56.2629 -43.0763 113.2972
REMARK 3 T TENSOR
REMARK 3 T11: 0.8766 T22: 0.7791
REMARK 3 T33: 0.5030 T12: 0.2944
REMARK 3 T13: -0.0040 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 7.2027 L22: 6.3430
REMARK 3 L33: 4.7346 L12: 2.2188
REMARK 3 L13: 1.9413 L23: 2.9102
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: -1.0442 S13: 0.3249
REMARK 3 S21: 0.8492 S22: -0.0461 S23: -0.2298
REMARK 3 S31: 0.5034 S32: 0.2371 S33: -0.0226
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4GX1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000074739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 78
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97921
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72260
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.978
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13-18% PEG 3350, 250-500MM KSCN, 100MM
REMARK 280 CHES, PH 9.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 117.16150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.72100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 117.16150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 55.72100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 81620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 81800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -116.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -116.34849
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 116.63313
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 K K A 601 LIES ON A SPECIAL POSITION.
REMARK 375 K K A 602 LIES ON A SPECIAL POSITION.
REMARK 375 K K A 603 LIES ON A SPECIAL POSITION.
REMARK 375 K K B 601 LIES ON A SPECIAL POSITION.
REMARK 375 K K B 602 LIES ON A SPECIAL POSITION.
REMARK 375 K K B 603 LIES ON A SPECIAL POSITION.
REMARK 375 K K C 601 LIES ON A SPECIAL POSITION.
REMARK 375 K K C 602 LIES ON A SPECIAL POSITION.
REMARK 375 K K C 603 LIES ON A SPECIAL POSITION.
REMARK 375 K K D 601 LIES ON A SPECIAL POSITION.
REMARK 375 K K D 602 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 4
REMARK 465 GLN A 5
REMARK 465 ARG A 6
REMARK 465 GLY A 7
REMARK 465 SER A 8
REMARK 465 ALA A 9
REMARK 465 TYR A 10
REMARK 465 PHE A 11
REMARK 465 LEU A 12
REMARK 465 ARG A 13
REMARK 465 GLY A 14
REMARK 465 ARG A 15
REMARK 465 ALA A 16
REMARK 465 ARG A 17
REMARK 465 CYS A 262
REMARK 465 GLY A 263
REMARK 465 ALA A 264
REMARK 465 LEU A 265
REMARK 465 ALA A 266
REMARK 465 HIS A 267
REMARK 465 ILE A 268
REMARK 465 LEU A 269
REMARK 465 ASP A 270
REMARK 465 SER A 271
REMARK 465 PHE A 272
REMARK 465 GLY A 273
REMARK 465 ASN A 274
REMARK 465 LEU A 275
REMARK 465 GLN A 276
REMARK 465 ILE A 277
REMARK 465 ALA A 278
REMARK 465 GLU A 279
REMARK 465 LEU A 280
REMARK 465 PRO A 281
REMARK 465 VAL A 282
REMARK 465 HIS A 283
REMARK 465 GLY A 284
REMARK 465 THR A 285
REMARK 465 PRO A 286
REMARK 465 PHE A 287
REMARK 465 ALA A 288
REMARK 465 GLY A 289
REMARK 465 LYS A 290
REMARK 465 THR A 291
REMARK 465 ILE A 292
REMARK 465 GLY A 293
REMARK 465 GLU A 294
REMARK 465 SER A 295
REMARK 465 GLY A 296
REMARK 465 ILE A 297
REMARK 465 ARG A 298
REMARK 465 GLN A 299
REMARK 465 ARG A 300
REMARK 465 THR A 301
REMARK 465 GLY A 302
REMARK 465 LEU A 303
REMARK 465 SER A 304
REMARK 465 ILE A 305
REMARK 465 ILE A 306
REMARK 465 GLY A 307
REMARK 465 VAL A 308
REMARK 465 TRP A 309
REMARK 465 GLU A 310
REMARK 465 ARG A 311
REMARK 465 GLY A 312
REMARK 465 SER A 313
REMARK 465 LEU A 314
REMARK 465 THR A 315
REMARK 465 THR A 316
REMARK 465 PRO A 317
REMARK 465 GLN A 318
REMARK 465 ARG A 319
REMARK 465 GLU A 320
REMARK 465 THR A 321
REMARK 465 VAL A 322
REMARK 465 LEU A 323
REMARK 465 THR A 324
REMARK 465 GLU A 325
REMARK 465 GLN A 326
REMARK 465 SER A 327
REMARK 465 LEU A 328
REMARK 465 LEU A 329
REMARK 465 VAL A 330
REMARK 465 LEU A 331
REMARK 465 ALA A 332
REMARK 465 GLY A 333
REMARK 465 THR A 334
REMARK 465 LYS A 335
REMARK 465 SER A 336
REMARK 465 GLN A 337
REMARK 465 LEU A 338
REMARK 465 ALA A 339
REMARK 465 ALA A 340
REMARK 465 LEU A 341
REMARK 465 GLU A 342
REMARK 465 TYR A 343
REMARK 465 LEU A 344
REMARK 465 ILE A 345
REMARK 465 GLY A 346
REMARK 465 GLU A 347
REMARK 465 ALA A 348
REMARK 465 PRO A 349
REMARK 465 SER A 482
REMARK 465 ALA A 483
REMARK 465 PHE A 484
REMARK 465 LEU A 485
REMARK 465 SER A 486
REMARK 465 GLU A 487
REMARK 465 GLY A 488
REMARK 465 MET A 489
REMARK 465 ALA A 490
REMARK 465 VAL A 491
REMARK 465 PHE A 492
REMARK 465 ARG A 493
REMARK 465 ARG A 494
REMARK 465 PRO A 495
REMARK 465 LEU A 496
REMARK 465 PRO A 497
REMARK 465 PRO A 498
REMARK 465 ALA A 499
REMARK 465 MET A 500
REMARK 465 ALA A 501
REMARK 465 GLY A 502
REMARK 465 LYS A 503
REMARK 465 THR A 504
REMARK 465 ILE A 505
REMARK 465 ALA A 506
REMARK 465 GLU A 507
REMARK 465 THR A 508
REMARK 465 ARG A 509
REMARK 465 LEU A 510
REMARK 465 ARG A 511
REMARK 465 PRO A 512
REMARK 465 LEU A 513
REMARK 465 THR A 514
REMARK 465 GLY A 515
REMARK 465 CYS A 516
REMARK 465 SER A 517
REMARK 465 ILE A 518
REMARK 465 VAL A 519
REMARK 465 ALA A 520
REMARK 465 ILE A 521
REMARK 465 GLU A 522
REMARK 465 ALA A 523
REMARK 465 PRO A 524
REMARK 465 ASP A 525
REMARK 465 ARG A 526
REMARK 465 ALA A 527
REMARK 465 ASP A 528
REMARK 465 ILE A 529
REMARK 465 LEU A 530
REMARK 465 ILE A 531
REMARK 465 SER A 532
REMARK 465 PRO A 533
REMARK 465 PRO A 534
REMARK 465 PRO A 535
REMARK 465 GLU A 536
REMARK 465 THR A 537
REMARK 465 ILE A 538
REMARK 465 LEU A 539
REMARK 465 ALA A 540
REMARK 465 GLU A 541
REMARK 465 GLY A 542
REMARK 465 ALA A 543
REMARK 465 ARG A 544
REMARK 465 LEU A 545
REMARK 465 ILE A 546
REMARK 465 LEU A 547
REMARK 465 ILE A 548
REMARK 465 GLY A 549
REMARK 465 THR A 550
REMARK 465 SER A 551
REMARK 465 GLU A 552
REMARK 465 GLN A 553
REMARK 465 GLU A 554
REMARK 465 LYS A 555
REMARK 465 THR A 556
REMARK 465 PHE A 557
REMARK 465 ASP A 558
REMARK 465 GLN A 559
REMARK 465 THR A 560
REMARK 465 ILE A 561
REMARK 465 ALA A 562
REMARK 465 ALA A 563
REMARK 465 ARG A 564
REMARK 465 LEU A 565
REMARK 465 VAL A 566
REMARK 465 PRO A 567
REMARK 465 ARG A 568
REMARK 465 MET B 4
REMARK 465 GLN B 5
REMARK 465 ARG B 6
REMARK 465 GLY B 7
REMARK 465 SER B 8
REMARK 465 ALA B 9
REMARK 465 TYR B 10
REMARK 465 PHE B 11
REMARK 465 LEU B 12
REMARK 465 ARG B 13
REMARK 465 GLY B 14
REMARK 465 ARG B 15
REMARK 465 ALA B 16
REMARK 465 ARG B 17
REMARK 465 LEU B 565
REMARK 465 VAL B 566
REMARK 465 PRO B 567
REMARK 465 ARG B 568
REMARK 465 MET C 4
REMARK 465 GLN C 5
REMARK 465 ARG C 6
REMARK 465 GLY C 7
REMARK 465 SER C 8
REMARK 465 ALA C 9
REMARK 465 TYR C 10
REMARK 465 PHE C 11
REMARK 465 LEU C 12
REMARK 465 ARG C 13
REMARK 465 GLY C 14
REMARK 465 ARG C 15
REMARK 465 ALA C 16
REMARK 465 ARG C 17
REMARK 465 GLN C 18
REMARK 465 LEU C 565
REMARK 465 VAL C 566
REMARK 465 PRO C 567
REMARK 465 ARG C 568
REMARK 465 MET D 4
REMARK 465 GLN D 5
REMARK 465 ARG D 6
REMARK 465 GLY D 7
REMARK 465 SER D 8
REMARK 465 ALA D 9
REMARK 465 TYR D 10
REMARK 465 PHE D 11
REMARK 465 LEU D 12
REMARK 465 ARG D 13
REMARK 465 GLY D 14
REMARK 465 ARG D 15
REMARK 465 ALA D 16
REMARK 465 ARG D 17
REMARK 465 CYS D 262
REMARK 465 GLY D 263
REMARK 465 ALA D 264
REMARK 465 LEU D 265
REMARK 465 ALA D 266
REMARK 465 HIS D 267
REMARK 465 ILE D 268
REMARK 465 LEU D 269
REMARK 465 ASP D 270
REMARK 465 SER D 271
REMARK 465 PHE D 272
REMARK 465 GLY D 273
REMARK 465 ASN D 274
REMARK 465 LEU D 275
REMARK 465 GLN D 276
REMARK 465 ILE D 277
REMARK 465 ALA D 278
REMARK 465 GLU D 279
REMARK 465 LEU D 280
REMARK 465 PRO D 281
REMARK 465 VAL D 282
REMARK 465 HIS D 283
REMARK 465 GLY D 284
REMARK 465 THR D 285
REMARK 465 PRO D 286
REMARK 465 PHE D 287
REMARK 465 ALA D 288
REMARK 465 GLY D 289
REMARK 465 LYS D 290
REMARK 465 THR D 291
REMARK 465 ILE D 292
REMARK 465 GLY D 293
REMARK 465 GLU D 294
REMARK 465 SER D 295
REMARK 465 GLY D 296
REMARK 465 ILE D 297
REMARK 465 ARG D 298
REMARK 465 GLN D 299
REMARK 465 ARG D 300
REMARK 465 THR D 301
REMARK 465 GLY D 302
REMARK 465 LEU D 303
REMARK 465 SER D 304
REMARK 465 ILE D 305
REMARK 465 ILE D 306
REMARK 465 GLY D 307
REMARK 465 VAL D 308
REMARK 465 TRP D 309
REMARK 465 GLU D 310
REMARK 465 ARG D 311
REMARK 465 GLY D 312
REMARK 465 SER D 313
REMARK 465 LEU D 314
REMARK 465 THR D 315
REMARK 465 THR D 316
REMARK 465 PRO D 317
REMARK 465 GLN D 318
REMARK 465 ARG D 319
REMARK 465 GLU D 320
REMARK 465 THR D 321
REMARK 465 VAL D 322
REMARK 465 LEU D 323
REMARK 465 THR D 324
REMARK 465 GLU D 325
REMARK 465 GLN D 326
REMARK 465 SER D 327
REMARK 465 LEU D 328
REMARK 465 LEU D 329
REMARK 465 VAL D 330
REMARK 465 LEU D 331
REMARK 465 ALA D 332
REMARK 465 GLY D 333
REMARK 465 THR D 334
REMARK 465 LYS D 335
REMARK 465 SER D 336
REMARK 465 GLN D 337
REMARK 465 LEU D 338
REMARK 465 ALA D 339
REMARK 465 ALA D 340
REMARK 465 LEU D 341
REMARK 465 GLU D 342
REMARK 465 TYR D 343
REMARK 465 LEU D 344
REMARK 465 ILE D 345
REMARK 465 GLY D 346
REMARK 465 GLU D 347
REMARK 465 ALA D 348
REMARK 465 PRO D 349
REMARK 465 GLU D 350
REMARK 465 ALA D 483
REMARK 465 PHE D 484
REMARK 465 LEU D 485
REMARK 465 SER D 486
REMARK 465 GLU D 487
REMARK 465 GLY D 488
REMARK 465 MET D 489
REMARK 465 ALA D 490
REMARK 465 VAL D 491
REMARK 465 PHE D 492
REMARK 465 ARG D 493
REMARK 465 ARG D 494
REMARK 465 PRO D 495
REMARK 465 LEU D 496
REMARK 465 PRO D 497
REMARK 465 PRO D 498
REMARK 465 ALA D 499
REMARK 465 MET D 500
REMARK 465 ALA D 501
REMARK 465 GLY D 502
REMARK 465 LYS D 503
REMARK 465 THR D 504
REMARK 465 ILE D 505
REMARK 465 ALA D 506
REMARK 465 GLU D 507
REMARK 465 THR D 508
REMARK 465 ARG D 509
REMARK 465 LEU D 510
REMARK 465 ARG D 511
REMARK 465 PRO D 512
REMARK 465 LEU D 513
REMARK 465 THR D 514
REMARK 465 GLY D 515
REMARK 465 CYS D 516
REMARK 465 SER D 517
REMARK 465 ILE D 518
REMARK 465 VAL D 519
REMARK 465 ALA D 520
REMARK 465 ILE D 521
REMARK 465 GLU D 522
REMARK 465 ALA D 523
REMARK 465 PRO D 524
REMARK 465 ASP D 525
REMARK 465 ARG D 526
REMARK 465 ALA D 527
REMARK 465 ASP D 528
REMARK 465 ILE D 529
REMARK 465 LEU D 530
REMARK 465 ILE D 531
REMARK 465 SER D 532
REMARK 465 PRO D 533
REMARK 465 PRO D 534
REMARK 465 PRO D 535
REMARK 465 GLU D 536
REMARK 465 THR D 537
REMARK 465 ILE D 538
REMARK 465 LEU D 539
REMARK 465 ALA D 540
REMARK 465 GLU D 541
REMARK 465 GLY D 542
REMARK 465 ALA D 543
REMARK 465 ARG D 544
REMARK 465 LEU D 545
REMARK 465 ILE D 546
REMARK 465 LEU D 547
REMARK 465 ILE D 548
REMARK 465 GLY D 549
REMARK 465 THR D 550
REMARK 465 SER D 551
REMARK 465 GLU D 552
REMARK 465 GLN D 553
REMARK 465 GLU D 554
REMARK 465 LYS D 555
REMARK 465 THR D 556
REMARK 465 PHE D 557
REMARK 465 ASP D 558
REMARK 465 GLN D 559
REMARK 465 THR D 560
REMARK 465 ILE D 561
REMARK 465 ALA D 562
REMARK 465 ALA D 563
REMARK 465 ARG D 564
REMARK 465 LEU D 565
REMARK 465 VAL D 566
REMARK 465 PRO D 567
REMARK 465 ARG D 568
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG B 564 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 564 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O1 PO4 C 610 O HOH C 748 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ILE A 98 -63.86 -125.34
REMARK 500 GLN A 172 92.25 -65.45
REMARK 500 PRO A 230 -27.04 -37.96
REMARK 500 THR A 260 -77.01 -109.80
REMARK 500 ASN A 389 33.04 -157.76
REMARK 500 ILE B 98 -70.06 -117.38
REMARK 500 GLN B 172 46.83 -103.28
REMARK 500 GLU B 173 96.66 -66.95
REMARK 500 ILE B 268 -64.77 -101.32
REMARK 500 GLN B 402 -22.75 71.08
REMARK 500 PHE B 557 -69.33 -92.20
REMARK 500 ILE C 98 -68.25 -123.62
REMARK 500 PHE C 108 16.77 -142.85
REMARK 500 LEU C 117 -76.03 -86.76
REMARK 500 ASN C 274 -100.84 -107.55
REMARK 500 THR C 301 -48.86 -130.43
REMARK 500 PRO C 374 98.98 -41.79
REMARK 500 HIS C 479 30.51 -92.85
REMARK 500 PRO C 524 -86.77 -38.97
REMARK 500 ASP C 525 38.15 -85.71
REMARK 500 THR D 68 6.73 80.26
REMARK 500 ILE D 98 -67.64 -124.66
REMARK 500 ARG D 116 -15.51 -141.14
REMARK 500 PRO D 374 95.95 -54.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 602 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 68 O
REMARK 620 2 LEU A 69 O 62.3
REMARK 620 3 THR B 68 O 82.6 85.2
REMARK 620 4 LEU B 69 O 129.3 75.1 67.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 601 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 69 O
REMARK 620 2 GLY A 70 O 81.2
REMARK 620 3 LEU B 69 O 74.1 129.7
REMARK 620 4 GLY B 70 O 97.1 67.7 72.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 601 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 70 O
REMARK 620 2 PHE A 71 O 68.3
REMARK 620 3 GLY B 70 O 70.3 85.6
REMARK 620 4 PHE B 71 O 128.4 77.9 69.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 604 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 359 NE2
REMARK 620 2 CYS A 364 SG 108.9
REMARK 620 3 CYS A 388 SG 109.6 108.7
REMARK 620 4 HIS A 391 ND1 106.1 101.7 121.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 605 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 449 O
REMARK 620 2 ASN A 450 OD1 90.8
REMARK 620 3 GLN A 453 OE1 65.6 116.4
REMARK 620 4 THR B 183 O 105.0 105.6 136.6
REMARK 620 5 ASN B 210 OD1 157.5 70.3 111.2 92.1
REMARK 620 6 THR B 214 OG1 135.8 131.6 81.8 78.2 61.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 604 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 359 NE2
REMARK 620 2 CYS B 364 SG 118.0
REMARK 620 3 CYS B 388 SG 110.7 102.4
REMARK 620 4 HIS B 391 ND1 106.9 108.1 110.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 605 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 449 O
REMARK 620 2 GLN B 453 OE1 69.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 601 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 68 O
REMARK 620 2 LEU C 69 O 65.3
REMARK 620 3 THR D 68 O 85.8 67.9
REMARK 620 4 LEU D 69 O 121.5 57.0 65.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 602 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU C 69 O
REMARK 620 2 GLY C 70 O 71.2
REMARK 620 3 LEU D 69 O 67.4 127.6
REMARK 620 4 GLY D 70 O 81.8 70.4 73.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 70 O
REMARK 620 2 PHE C 71 O 67.6
REMARK 620 3 GLY D 70 O 73.0 83.0
REMARK 620 4 PHE D 71 O 129.6 72.2 73.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 605 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 183 O
REMARK 620 2 ASN C 210 OD1 100.5
REMARK 620 3 THR C 214 OG1 70.9 63.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 604 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 359 NE2
REMARK 620 2 CYS C 364 SG 115.0
REMARK 620 3 CYS C 388 SG 104.4 103.6
REMARK 620 4 HIS C 391 ND1 117.9 97.2 118.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 606 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 449 O
REMARK 620 2 ASN C 450 OD1 79.5
REMARK 620 3 GLN C 453 OE1 61.3 108.1
REMARK 620 4 THR D 183 O 93.4 81.2 149.5
REMARK 620 5 ASN D 210 OD1 141.8 73.8 101.8 108.8
REMARK 620 6 THR D 214 OG1 135.6 140.5 83.4 108.3 66.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 603 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 359 NE2
REMARK 620 2 CYS D 364 SG 110.0
REMARK 620 3 CYS D 388 SG 109.8 111.5
REMARK 620 N 1 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GVL RELATED DB: PDB
REMARK 900 GSUK GATING RING
REMARK 900 RELATED ID: 4GX0 RELATED DB: PDB
REMARK 900 GSUK L97D MUTANT
REMARK 900 RELATED ID: 4GX2 RELATED DB: PDB
REMARK 900 RELATED ID: 4GX5 RELATED DB: PDB
DBREF 4GX1 A 9 564 UNP Q74FS9 Q74FS9_GEOSL 9 564
DBREF 4GX1 B 9 564 UNP Q74FS9 Q74FS9_GEOSL 9 564
DBREF 4GX1 C 9 564 UNP Q74FS9 Q74FS9_GEOSL 9 564
DBREF 4GX1 D 9 564 UNP Q74FS9 Q74FS9_GEOSL 9 564
SEQADV 4GX1 MET A 4 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 GLN A 5 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 ARG A 6 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 GLY A 7 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 SER A 8 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 ALA A 52 UNP Q74FS9 GLU 52 ENGINEERED MUTATION
SEQADV 4GX1 GLU A 77 UNP Q74FS9 GLN 77 ENGINEERED MUTATION
SEQADV 4GX1 ASP A 97 UNP Q74FS9 LEU 97 ENGINEERED MUTATION
SEQADV 4GX1 LEU A 565 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 VAL A 566 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 PRO A 567 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 ARG A 568 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 MET B 4 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 GLN B 5 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 ARG B 6 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 GLY B 7 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 SER B 8 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 ALA B 52 UNP Q74FS9 GLU 52 ENGINEERED MUTATION
SEQADV 4GX1 GLU B 77 UNP Q74FS9 GLN 77 ENGINEERED MUTATION
SEQADV 4GX1 ASP B 97 UNP Q74FS9 LEU 97 ENGINEERED MUTATION
SEQADV 4GX1 LEU B 565 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 VAL B 566 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 PRO B 567 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 ARG B 568 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 MET C 4 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 GLN C 5 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 ARG C 6 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 GLY C 7 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 SER C 8 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 ALA C 52 UNP Q74FS9 GLU 52 ENGINEERED MUTATION
SEQADV 4GX1 GLU C 77 UNP Q74FS9 GLN 77 ENGINEERED MUTATION
SEQADV 4GX1 ASP C 97 UNP Q74FS9 LEU 97 ENGINEERED MUTATION
SEQADV 4GX1 LEU C 565 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 VAL C 566 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 PRO C 567 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 ARG C 568 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 MET D 4 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 GLN D 5 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 ARG D 6 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 GLY D 7 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 SER D 8 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 ALA D 52 UNP Q74FS9 GLU 52 ENGINEERED MUTATION
SEQADV 4GX1 GLU D 77 UNP Q74FS9 GLN 77 ENGINEERED MUTATION
SEQADV 4GX1 ASP D 97 UNP Q74FS9 LEU 97 ENGINEERED MUTATION
SEQADV 4GX1 LEU D 565 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 VAL D 566 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 PRO D 567 UNP Q74FS9 EXPRESSION TAG
SEQADV 4GX1 ARG D 568 UNP Q74FS9 EXPRESSION TAG
SEQRES 1 A 565 MET GLN ARG GLY SER ALA TYR PHE LEU ARG GLY ARG ALA
SEQRES 2 A 565 ARG GLN ASN LEU LYS VAL LEU LEU LEU TYR CYS ALA PHE
SEQRES 3 A 565 LEU LEU VAL MET LEU LEU ALA TYR ALA SER ILE PHE ARG
SEQRES 4 A 565 TYR LEU MET TRP HIS LEU GLU GLY ARG ALA TYR SER PHE
SEQRES 5 A 565 MET ALA GLY ILE TYR TRP THR ILE THR VAL MET THR THR
SEQRES 6 A 565 LEU GLY PHE GLY ASP ILE THR PHE GLU SER ASP ALA GLY
SEQRES 7 A 565 TYR LEU PHE ALA SER ILE VAL THR VAL SER GLY VAL ILE
SEQRES 8 A 565 PHE LEU ASP ILE ILE LEU PRO PHE GLY PHE VAL SER MET
SEQRES 9 A 565 PHE LEU ALA PRO TRP ILE GLU ARG ARG LEU ARG TYR HIS
SEQRES 10 A 565 PRO THR ILE GLU LEU PRO ASP ASP THR ARG GLY HIS ILE
SEQRES 11 A 565 LEU ILE PHE GLY ILE ASP PRO ILE THR ARG THR LEU ILE
SEQRES 12 A 565 ARG LYS LEU GLU SER ARG ASN HIS LEU PHE VAL VAL VAL
SEQRES 13 A 565 THR ASP ASN TYR ASP GLN ALA LEU HIS LEU GLU GLU GLN
SEQRES 14 A 565 GLU GLY PHE LYS VAL VAL TYR GLY SER PRO THR ASP ALA
SEQRES 15 A 565 HIS VAL LEU ALA GLY LEU ARG VAL ALA ALA ALA ARG SER
SEQRES 16 A 565 ILE ILE ALA ASN LEU SER ASP PRO ASP ASN ALA ASN LEU
SEQRES 17 A 565 CYS LEU THR VAL ARG SER LEU CYS GLN THR PRO ILE ILE
SEQRES 18 A 565 ALA VAL VAL LYS GLU PRO VAL HIS GLY GLU LEU LEU ARG
SEQRES 19 A 565 LEU ALA GLY ALA ASN GLN VAL VAL PRO LEU THR ARG ILE
SEQRES 20 A 565 LEU GLY ARG TYR LEU GLY ILE ARG ALA THR THR CYS GLY
SEQRES 21 A 565 ALA LEU ALA HIS ILE LEU ASP SER PHE GLY ASN LEU GLN
SEQRES 22 A 565 ILE ALA GLU LEU PRO VAL HIS GLY THR PRO PHE ALA GLY
SEQRES 23 A 565 LYS THR ILE GLY GLU SER GLY ILE ARG GLN ARG THR GLY
SEQRES 24 A 565 LEU SER ILE ILE GLY VAL TRP GLU ARG GLY SER LEU THR
SEQRES 25 A 565 THR PRO GLN ARG GLU THR VAL LEU THR GLU GLN SER LEU
SEQRES 26 A 565 LEU VAL LEU ALA GLY THR LYS SER GLN LEU ALA ALA LEU
SEQRES 27 A 565 GLU TYR LEU ILE GLY GLU ALA PRO GLU ASP GLU LEU ILE
SEQRES 28 A 565 PHE ILE ILE GLY HIS GLY ARG ILE GLY CYS ALA ALA ALA
SEQRES 29 A 565 ALA PHE LEU ASP ARG LYS PRO VAL PRO PHE ILE LEU ILE
SEQRES 30 A 565 ASP ARG GLN GLU SER PRO VAL CYS ASN ASP HIS VAL VAL
SEQRES 31 A 565 VAL TYR GLY ASP ALA THR VAL GLY GLN THR LEU ARG GLN
SEQRES 32 A 565 ALA GLY ILE ASP ARG ALA SER GLY ILE ILE VAL THR THR
SEQRES 33 A 565 ASN ASP ASP SER THR ASN ILE PHE LEU THR LEU ALA CYS
SEQRES 34 A 565 ARG HIS LEU HIS SER HIS ILE ARG ILE VAL ALA ARG ALA
SEQRES 35 A 565 ASN GLY GLU GLU ASN VAL ASP GLN LEU TYR ALA ALA GLY
SEQRES 36 A 565 ALA ASP PHE VAL VAL SER ASN ALA SER VAL GLY ALA ASN
SEQRES 37 A 565 ILE LEU GLY ASN LEU LEU GLU HIS LYS GLU SER ALA PHE
SEQRES 38 A 565 LEU SER GLU GLY MET ALA VAL PHE ARG ARG PRO LEU PRO
SEQRES 39 A 565 PRO ALA MET ALA GLY LYS THR ILE ALA GLU THR ARG LEU
SEQRES 40 A 565 ARG PRO LEU THR GLY CYS SER ILE VAL ALA ILE GLU ALA
SEQRES 41 A 565 PRO ASP ARG ALA ASP ILE LEU ILE SER PRO PRO PRO GLU
SEQRES 42 A 565 THR ILE LEU ALA GLU GLY ALA ARG LEU ILE LEU ILE GLY
SEQRES 43 A 565 THR SER GLU GLN GLU LYS THR PHE ASP GLN THR ILE ALA
SEQRES 44 A 565 ALA ARG LEU VAL PRO ARG
SEQRES 1 B 565 MET GLN ARG GLY SER ALA TYR PHE LEU ARG GLY ARG ALA
SEQRES 2 B 565 ARG GLN ASN LEU LYS VAL LEU LEU LEU TYR CYS ALA PHE
SEQRES 3 B 565 LEU LEU VAL MET LEU LEU ALA TYR ALA SER ILE PHE ARG
SEQRES 4 B 565 TYR LEU MET TRP HIS LEU GLU GLY ARG ALA TYR SER PHE
SEQRES 5 B 565 MET ALA GLY ILE TYR TRP THR ILE THR VAL MET THR THR
SEQRES 6 B 565 LEU GLY PHE GLY ASP ILE THR PHE GLU SER ASP ALA GLY
SEQRES 7 B 565 TYR LEU PHE ALA SER ILE VAL THR VAL SER GLY VAL ILE
SEQRES 8 B 565 PHE LEU ASP ILE ILE LEU PRO PHE GLY PHE VAL SER MET
SEQRES 9 B 565 PHE LEU ALA PRO TRP ILE GLU ARG ARG LEU ARG TYR HIS
SEQRES 10 B 565 PRO THR ILE GLU LEU PRO ASP ASP THR ARG GLY HIS ILE
SEQRES 11 B 565 LEU ILE PHE GLY ILE ASP PRO ILE THR ARG THR LEU ILE
SEQRES 12 B 565 ARG LYS LEU GLU SER ARG ASN HIS LEU PHE VAL VAL VAL
SEQRES 13 B 565 THR ASP ASN TYR ASP GLN ALA LEU HIS LEU GLU GLU GLN
SEQRES 14 B 565 GLU GLY PHE LYS VAL VAL TYR GLY SER PRO THR ASP ALA
SEQRES 15 B 565 HIS VAL LEU ALA GLY LEU ARG VAL ALA ALA ALA ARG SER
SEQRES 16 B 565 ILE ILE ALA ASN LEU SER ASP PRO ASP ASN ALA ASN LEU
SEQRES 17 B 565 CYS LEU THR VAL ARG SER LEU CYS GLN THR PRO ILE ILE
SEQRES 18 B 565 ALA VAL VAL LYS GLU PRO VAL HIS GLY GLU LEU LEU ARG
SEQRES 19 B 565 LEU ALA GLY ALA ASN GLN VAL VAL PRO LEU THR ARG ILE
SEQRES 20 B 565 LEU GLY ARG TYR LEU GLY ILE ARG ALA THR THR CYS GLY
SEQRES 21 B 565 ALA LEU ALA HIS ILE LEU ASP SER PHE GLY ASN LEU GLN
SEQRES 22 B 565 ILE ALA GLU LEU PRO VAL HIS GLY THR PRO PHE ALA GLY
SEQRES 23 B 565 LYS THR ILE GLY GLU SER GLY ILE ARG GLN ARG THR GLY
SEQRES 24 B 565 LEU SER ILE ILE GLY VAL TRP GLU ARG GLY SER LEU THR
SEQRES 25 B 565 THR PRO GLN ARG GLU THR VAL LEU THR GLU GLN SER LEU
SEQRES 26 B 565 LEU VAL LEU ALA GLY THR LYS SER GLN LEU ALA ALA LEU
SEQRES 27 B 565 GLU TYR LEU ILE GLY GLU ALA PRO GLU ASP GLU LEU ILE
SEQRES 28 B 565 PHE ILE ILE GLY HIS GLY ARG ILE GLY CYS ALA ALA ALA
SEQRES 29 B 565 ALA PHE LEU ASP ARG LYS PRO VAL PRO PHE ILE LEU ILE
SEQRES 30 B 565 ASP ARG GLN GLU SER PRO VAL CYS ASN ASP HIS VAL VAL
SEQRES 31 B 565 VAL TYR GLY ASP ALA THR VAL GLY GLN THR LEU ARG GLN
SEQRES 32 B 565 ALA GLY ILE ASP ARG ALA SER GLY ILE ILE VAL THR THR
SEQRES 33 B 565 ASN ASP ASP SER THR ASN ILE PHE LEU THR LEU ALA CYS
SEQRES 34 B 565 ARG HIS LEU HIS SER HIS ILE ARG ILE VAL ALA ARG ALA
SEQRES 35 B 565 ASN GLY GLU GLU ASN VAL ASP GLN LEU TYR ALA ALA GLY
SEQRES 36 B 565 ALA ASP PHE VAL VAL SER ASN ALA SER VAL GLY ALA ASN
SEQRES 37 B 565 ILE LEU GLY ASN LEU LEU GLU HIS LYS GLU SER ALA PHE
SEQRES 38 B 565 LEU SER GLU GLY MET ALA VAL PHE ARG ARG PRO LEU PRO
SEQRES 39 B 565 PRO ALA MET ALA GLY LYS THR ILE ALA GLU THR ARG LEU
SEQRES 40 B 565 ARG PRO LEU THR GLY CYS SER ILE VAL ALA ILE GLU ALA
SEQRES 41 B 565 PRO ASP ARG ALA ASP ILE LEU ILE SER PRO PRO PRO GLU
SEQRES 42 B 565 THR ILE LEU ALA GLU GLY ALA ARG LEU ILE LEU ILE GLY
SEQRES 43 B 565 THR SER GLU GLN GLU LYS THR PHE ASP GLN THR ILE ALA
SEQRES 44 B 565 ALA ARG LEU VAL PRO ARG
SEQRES 1 C 565 MET GLN ARG GLY SER ALA TYR PHE LEU ARG GLY ARG ALA
SEQRES 2 C 565 ARG GLN ASN LEU LYS VAL LEU LEU LEU TYR CYS ALA PHE
SEQRES 3 C 565 LEU LEU VAL MET LEU LEU ALA TYR ALA SER ILE PHE ARG
SEQRES 4 C 565 TYR LEU MET TRP HIS LEU GLU GLY ARG ALA TYR SER PHE
SEQRES 5 C 565 MET ALA GLY ILE TYR TRP THR ILE THR VAL MET THR THR
SEQRES 6 C 565 LEU GLY PHE GLY ASP ILE THR PHE GLU SER ASP ALA GLY
SEQRES 7 C 565 TYR LEU PHE ALA SER ILE VAL THR VAL SER GLY VAL ILE
SEQRES 8 C 565 PHE LEU ASP ILE ILE LEU PRO PHE GLY PHE VAL SER MET
SEQRES 9 C 565 PHE LEU ALA PRO TRP ILE GLU ARG ARG LEU ARG TYR HIS
SEQRES 10 C 565 PRO THR ILE GLU LEU PRO ASP ASP THR ARG GLY HIS ILE
SEQRES 11 C 565 LEU ILE PHE GLY ILE ASP PRO ILE THR ARG THR LEU ILE
SEQRES 12 C 565 ARG LYS LEU GLU SER ARG ASN HIS LEU PHE VAL VAL VAL
SEQRES 13 C 565 THR ASP ASN TYR ASP GLN ALA LEU HIS LEU GLU GLU GLN
SEQRES 14 C 565 GLU GLY PHE LYS VAL VAL TYR GLY SER PRO THR ASP ALA
SEQRES 15 C 565 HIS VAL LEU ALA GLY LEU ARG VAL ALA ALA ALA ARG SER
SEQRES 16 C 565 ILE ILE ALA ASN LEU SER ASP PRO ASP ASN ALA ASN LEU
SEQRES 17 C 565 CYS LEU THR VAL ARG SER LEU CYS GLN THR PRO ILE ILE
SEQRES 18 C 565 ALA VAL VAL LYS GLU PRO VAL HIS GLY GLU LEU LEU ARG
SEQRES 19 C 565 LEU ALA GLY ALA ASN GLN VAL VAL PRO LEU THR ARG ILE
SEQRES 20 C 565 LEU GLY ARG TYR LEU GLY ILE ARG ALA THR THR CYS GLY
SEQRES 21 C 565 ALA LEU ALA HIS ILE LEU ASP SER PHE GLY ASN LEU GLN
SEQRES 22 C 565 ILE ALA GLU LEU PRO VAL HIS GLY THR PRO PHE ALA GLY
SEQRES 23 C 565 LYS THR ILE GLY GLU SER GLY ILE ARG GLN ARG THR GLY
SEQRES 24 C 565 LEU SER ILE ILE GLY VAL TRP GLU ARG GLY SER LEU THR
SEQRES 25 C 565 THR PRO GLN ARG GLU THR VAL LEU THR GLU GLN SER LEU
SEQRES 26 C 565 LEU VAL LEU ALA GLY THR LYS SER GLN LEU ALA ALA LEU
SEQRES 27 C 565 GLU TYR LEU ILE GLY GLU ALA PRO GLU ASP GLU LEU ILE
SEQRES 28 C 565 PHE ILE ILE GLY HIS GLY ARG ILE GLY CYS ALA ALA ALA
SEQRES 29 C 565 ALA PHE LEU ASP ARG LYS PRO VAL PRO PHE ILE LEU ILE
SEQRES 30 C 565 ASP ARG GLN GLU SER PRO VAL CYS ASN ASP HIS VAL VAL
SEQRES 31 C 565 VAL TYR GLY ASP ALA THR VAL GLY GLN THR LEU ARG GLN
SEQRES 32 C 565 ALA GLY ILE ASP ARG ALA SER GLY ILE ILE VAL THR THR
SEQRES 33 C 565 ASN ASP ASP SER THR ASN ILE PHE LEU THR LEU ALA CYS
SEQRES 34 C 565 ARG HIS LEU HIS SER HIS ILE ARG ILE VAL ALA ARG ALA
SEQRES 35 C 565 ASN GLY GLU GLU ASN VAL ASP GLN LEU TYR ALA ALA GLY
SEQRES 36 C 565 ALA ASP PHE VAL VAL SER ASN ALA SER VAL GLY ALA ASN
SEQRES 37 C 565 ILE LEU GLY ASN LEU LEU GLU HIS LYS GLU SER ALA PHE
SEQRES 38 C 565 LEU SER GLU GLY MET ALA VAL PHE ARG ARG PRO LEU PRO
SEQRES 39 C 565 PRO ALA MET ALA GLY LYS THR ILE ALA GLU THR ARG LEU
SEQRES 40 C 565 ARG PRO LEU THR GLY CYS SER ILE VAL ALA ILE GLU ALA
SEQRES 41 C 565 PRO ASP ARG ALA ASP ILE LEU ILE SER PRO PRO PRO GLU
SEQRES 42 C 565 THR ILE LEU ALA GLU GLY ALA ARG LEU ILE LEU ILE GLY
SEQRES 43 C 565 THR SER GLU GLN GLU LYS THR PHE ASP GLN THR ILE ALA
SEQRES 44 C 565 ALA ARG LEU VAL PRO ARG
SEQRES 1 D 565 MET GLN ARG GLY SER ALA TYR PHE LEU ARG GLY ARG ALA
SEQRES 2 D 565 ARG GLN ASN LEU LYS VAL LEU LEU LEU TYR CYS ALA PHE
SEQRES 3 D 565 LEU LEU VAL MET LEU LEU ALA TYR ALA SER ILE PHE ARG
SEQRES 4 D 565 TYR LEU MET TRP HIS LEU GLU GLY ARG ALA TYR SER PHE
SEQRES 5 D 565 MET ALA GLY ILE TYR TRP THR ILE THR VAL MET THR THR
SEQRES 6 D 565 LEU GLY PHE GLY ASP ILE THR PHE GLU SER ASP ALA GLY
SEQRES 7 D 565 TYR LEU PHE ALA SER ILE VAL THR VAL SER GLY VAL ILE
SEQRES 8 D 565 PHE LEU ASP ILE ILE LEU PRO PHE GLY PHE VAL SER MET
SEQRES 9 D 565 PHE LEU ALA PRO TRP ILE GLU ARG ARG LEU ARG TYR HIS
SEQRES 10 D 565 PRO THR ILE GLU LEU PRO ASP ASP THR ARG GLY HIS ILE
SEQRES 11 D 565 LEU ILE PHE GLY ILE ASP PRO ILE THR ARG THR LEU ILE
SEQRES 12 D 565 ARG LYS LEU GLU SER ARG ASN HIS LEU PHE VAL VAL VAL
SEQRES 13 D 565 THR ASP ASN TYR ASP GLN ALA LEU HIS LEU GLU GLU GLN
SEQRES 14 D 565 GLU GLY PHE LYS VAL VAL TYR GLY SER PRO THR ASP ALA
SEQRES 15 D 565 HIS VAL LEU ALA GLY LEU ARG VAL ALA ALA ALA ARG SER
SEQRES 16 D 565 ILE ILE ALA ASN LEU SER ASP PRO ASP ASN ALA ASN LEU
SEQRES 17 D 565 CYS LEU THR VAL ARG SER LEU CYS GLN THR PRO ILE ILE
SEQRES 18 D 565 ALA VAL VAL LYS GLU PRO VAL HIS GLY GLU LEU LEU ARG
SEQRES 19 D 565 LEU ALA GLY ALA ASN GLN VAL VAL PRO LEU THR ARG ILE
SEQRES 20 D 565 LEU GLY ARG TYR LEU GLY ILE ARG ALA THR THR CYS GLY
SEQRES 21 D 565 ALA LEU ALA HIS ILE LEU ASP SER PHE GLY ASN LEU GLN
SEQRES 22 D 565 ILE ALA GLU LEU PRO VAL HIS GLY THR PRO PHE ALA GLY
SEQRES 23 D 565 LYS THR ILE GLY GLU SER GLY ILE ARG GLN ARG THR GLY
SEQRES 24 D 565 LEU SER ILE ILE GLY VAL TRP GLU ARG GLY SER LEU THR
SEQRES 25 D 565 THR PRO GLN ARG GLU THR VAL LEU THR GLU GLN SER LEU
SEQRES 26 D 565 LEU VAL LEU ALA GLY THR LYS SER GLN LEU ALA ALA LEU
SEQRES 27 D 565 GLU TYR LEU ILE GLY GLU ALA PRO GLU ASP GLU LEU ILE
SEQRES 28 D 565 PHE ILE ILE GLY HIS GLY ARG ILE GLY CYS ALA ALA ALA
SEQRES 29 D 565 ALA PHE LEU ASP ARG LYS PRO VAL PRO PHE ILE LEU ILE
SEQRES 30 D 565 ASP ARG GLN GLU SER PRO VAL CYS ASN ASP HIS VAL VAL
SEQRES 31 D 565 VAL TYR GLY ASP ALA THR VAL GLY GLN THR LEU ARG GLN
SEQRES 32 D 565 ALA GLY ILE ASP ARG ALA SER GLY ILE ILE VAL THR THR
SEQRES 33 D 565 ASN ASP ASP SER THR ASN ILE PHE LEU THR LEU ALA CYS
SEQRES 34 D 565 ARG HIS LEU HIS SER HIS ILE ARG ILE VAL ALA ARG ALA
SEQRES 35 D 565 ASN GLY GLU GLU ASN VAL ASP GLN LEU TYR ALA ALA GLY
SEQRES 36 D 565 ALA ASP PHE VAL VAL SER ASN ALA SER VAL GLY ALA ASN
SEQRES 37 D 565 ILE LEU GLY ASN LEU LEU GLU HIS LYS GLU SER ALA PHE
SEQRES 38 D 565 LEU SER GLU GLY MET ALA VAL PHE ARG ARG PRO LEU PRO
SEQRES 39 D 565 PRO ALA MET ALA GLY LYS THR ILE ALA GLU THR ARG LEU
SEQRES 40 D 565 ARG PRO LEU THR GLY CYS SER ILE VAL ALA ILE GLU ALA
SEQRES 41 D 565 PRO ASP ARG ALA ASP ILE LEU ILE SER PRO PRO PRO GLU
SEQRES 42 D 565 THR ILE LEU ALA GLU GLY ALA ARG LEU ILE LEU ILE GLY
SEQRES 43 D 565 THR SER GLU GLN GLU LYS THR PHE ASP GLN THR ILE ALA
SEQRES 44 D 565 ALA ARG LEU VAL PRO ARG
HET K A 601 1
HET K A 602 1
HET K A 603 1
HET ZN A 604 1
HET CA A 605 1
HET ADP A 606 27
HET K B 601 1
HET K B 602 1
HET K B 603 1
HET ZN B 604 1
HET CA B 605 1
HET ADP B 606 27
HET GLC B 607 12
HET PO4 B 608 5
HET K C 601 1
HET K C 602 1
HET K C 603 1
HET ZN C 604 1
HET CA C 605 1
HET CA C 606 1
HET ADP C 607 27
HET GLC C 608 12
HET GLC C 609 12
HET PO4 C 610 5
HET K D 601 1
HET K D 602 1
HET ZN D 603 1
HET ADP D 604 27
HET GLC D 605 12
HETNAM K POTASSIUM ION
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM PO4 PHOSPHATE ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 5 K 11(K 1+)
FORMUL 8 ZN 4(ZN 2+)
FORMUL 9 CA 4(CA 2+)
FORMUL 10 ADP 4(C10 H15 N5 O10 P2)
FORMUL 17 GLC 4(C6 H12 O6)
FORMUL 18 PO4 2(O4 P 3-)
FORMUL 34 HOH *273(H2 O)
HELIX 1 1 GLN A 18 GLY A 50 1 33
HELIX 2 2 SER A 54 THR A 67 1 14
HELIX 3 3 SER A 78 ASP A 97 1 20
HELIX 4 4 ILE A 98 LEU A 109 1 12
HELIX 5 5 LEU A 109 LEU A 117 1 9
HELIX 6 6 ASP A 139 ARG A 147 1 9
HELIX 7 7 ASN A 162 GLN A 172 1 11
HELIX 8 8 ASP A 184 GLY A 190 1 7
HELIX 9 9 ARG A 192 ALA A 196 5 5
HELIX 10 10 SER A 204 CYS A 219 1 16
HELIX 11 11 GLU A 229 VAL A 231 5 3
HELIX 12 12 HIS A 232 GLY A 240 1 9
HELIX 13 13 PRO A 246 THR A 261 1 16
HELIX 14 14 GLY A 360 LYS A 373 1 14
HELIX 15 15 LEU A 404 GLY A 408 5 5
HELIX 16 16 ASP A 421 HIS A 436 1 16
HELIX 17 17 GLY A 447 GLU A 449 5 3
HELIX 18 18 ASN A 450 GLY A 458 1 9
HELIX 19 19 ASN A 465 GLU A 481 1 17
HELIX 20 20 ASN B 19 GLY B 50 1 32
HELIX 21 21 SER B 54 THR B 67 1 14
HELIX 22 22 SER B 78 ILE B 98 1 21
HELIX 23 23 ILE B 98 PHE B 108 1 11
HELIX 24 24 PHE B 108 ARG B 118 1 11
HELIX 25 25 ASP B 139 SER B 151 1 13
HELIX 26 26 ASN B 162 GLN B 172 1 11
HELIX 27 27 ASP B 184 LEU B 191 1 8
HELIX 28 28 ARG B 192 ALA B 196 5 5
HELIX 29 29 SER B 204 SER B 217 1 14
HELIX 30 30 GLU B 229 VAL B 231 5 3
HELIX 31 31 HIS B 232 GLY B 240 1 9
HELIX 32 32 PRO B 246 THR B 260 1 15
HELIX 33 33 THR B 291 GLY B 296 1 6
HELIX 34 34 GLY B 296 GLY B 302 1 7
HELIX 35 35 THR B 334 GLY B 346 1 13
HELIX 36 36 GLY B 360 ASP B 371 1 12
HELIX 37 37 LEU B 404 ALA B 412 5 9
HELIX 38 38 ASP B 421 HIS B 436 1 16
HELIX 39 39 GLY B 447 GLU B 449 5 3
HELIX 40 40 ASN B 450 GLY B 458 1 9
HELIX 41 41 ASN B 465 HIS B 479 1 15
HELIX 42 42 LYS B 480 ALA B 483 5 4
HELIX 43 43 PRO B 497 ALA B 501 5 5
HELIX 44 44 THR B 504 ARG B 509 1 6
HELIX 45 45 GLN B 559 ARG B 564 1 6
HELIX 46 46 LEU C 20 GLY C 50 1 31
HELIX 47 47 SER C 54 THR C 67 1 14
HELIX 48 48 SER C 78 ILE C 98 1 21
HELIX 49 49 ILE C 98 LEU C 109 1 12
HELIX 50 50 LEU C 109 LEU C 117 1 9
HELIX 51 51 ASP C 139 GLU C 150 1 12
HELIX 52 52 ASN C 162 GLN C 172 1 11
HELIX 53 53 ASP C 184 LEU C 191 1 8
HELIX 54 54 ARG C 192 ALA C 196 5 5
HELIX 55 55 SER C 204 SER C 217 1 14
HELIX 56 56 GLU C 229 VAL C 231 5 3
HELIX 57 57 HIS C 232 GLY C 240 1 9
HELIX 58 58 PRO C 246 THR C 260 1 15
HELIX 59 59 THR C 291 GLY C 296 1 6
HELIX 60 60 GLY C 296 GLY C 302 1 7
HELIX 61 61 THR C 334 GLY C 346 1 13
HELIX 62 62 GLY C 360 LYS C 373 1 14
HELIX 63 63 LEU C 404 ALA C 412 5 9
HELIX 64 64 ASP C 421 HIS C 436 1 16
HELIX 65 65 GLY C 447 GLU C 449 5 3
HELIX 66 66 ASN C 450 GLY C 458 1 9
HELIX 67 67 ASN C 465 HIS C 479 1 15
HELIX 68 68 HIS C 479 GLU C 487 1 9
HELIX 69 69 PRO C 497 ALA C 501 5 5
HELIX 70 70 ARG C 509 GLY C 515 1 7
HELIX 71 71 SER C 551 THR C 556 1 6
HELIX 72 72 THR C 556 ILE C 561 1 6
HELIX 73 73 ASN D 19 GLY D 50 1 32
HELIX 74 74 SER D 54 THR D 67 1 14
HELIX 75 75 SER D 78 ILE D 98 1 21
HELIX 76 76 ILE D 98 PHE D 108 1 11
HELIX 77 77 PHE D 108 LEU D 117 1 10
HELIX 78 78 ASP D 139 LEU D 149 1 11
HELIX 79 79 ASN D 162 GLN D 172 1 11
HELIX 80 80 ASP D 184 LEU D 191 1 8
HELIX 81 81 ARG D 192 ALA D 196 5 5
HELIX 82 82 SER D 204 CYS D 219 1 16
HELIX 83 83 GLU D 229 VAL D 231 5 3
HELIX 84 84 HIS D 232 GLY D 240 1 9
HELIX 85 85 PRO D 246 THR D 261 1 16
HELIX 86 86 GLY D 360 LYS D 373 1 14
HELIX 87 87 LEU D 404 ALA D 412 5 9
HELIX 88 88 ASP D 421 HIS D 436 1 16
HELIX 89 89 GLY D 447 GLU D 449 5 3
HELIX 90 90 ASN D 450 GLY D 458 1 9
HELIX 91 91 ASN D 465 SER D 482 1 18
SHEET 1 A 6 LYS A 176 TYR A 179 0
SHEET 2 A 6 PHE A 156 THR A 160 1 N VAL A 158 O LYS A 176
SHEET 3 A 6 ILE A 133 PHE A 136 1 N ILE A 135 O VAL A 157
SHEET 4 A 6 SER A 198 ALA A 201 1 O ILE A 200 N LEU A 134
SHEET 5 A 6 ILE A 223 VAL A 226 1 O ILE A 224 N ILE A 199
SHEET 6 A 6 GLN A 243 VAL A 245 1 O VAL A 245 N ALA A 225
SHEET 1 B 6 VAL A 393 TYR A 395 0
SHEET 2 B 6 PHE A 377 ASP A 381 1 N LEU A 379 O VAL A 394
SHEET 3 B 6 ILE A 354 ILE A 357 1 N ILE A 356 O ILE A 378
SHEET 4 B 6 GLY A 414 VAL A 417 1 O ILE A 416 N PHE A 355
SHEET 5 B 6 ARG A 440 ALA A 445 1 O VAL A 442 N ILE A 415
SHEET 6 B 6 PHE A 461 SER A 464 1 O VAL A 463 N ALA A 445
SHEET 1 C 6 LYS B 176 TYR B 179 0
SHEET 2 C 6 PHE B 156 THR B 160 1 N VAL B 158 O VAL B 178
SHEET 3 C 6 ILE B 133 PHE B 136 1 N ILE B 135 O VAL B 157
SHEET 4 C 6 SER B 198 ALA B 201 1 O ILE B 200 N LEU B 134
SHEET 5 C 6 ILE B 223 VAL B 226 1 O ILE B 224 N ALA B 201
SHEET 6 C 6 GLN B 243 VAL B 245 1 O VAL B 245 N ALA B 225
SHEET 1 D 5 ALA B 266 SER B 271 0
SHEET 2 D 5 LEU B 275 PRO B 281 -1 O ILE B 277 N ILE B 268
SHEET 3 D 5 LEU B 328 GLY B 333 -1 O LEU B 331 N ALA B 278
SHEET 4 D 5 SER B 304 GLU B 310 -1 N SER B 304 O ALA B 332
SHEET 5 D 5 SER B 313 THR B 315 -1 O THR B 315 N VAL B 308
SHEET 1 E 6 VAL B 393 TYR B 395 0
SHEET 2 E 6 PHE B 377 ASP B 381 1 N LEU B 379 O VAL B 394
SHEET 3 E 6 ILE B 354 ILE B 357 1 N ILE B 356 O ILE B 378
SHEET 4 E 6 GLY B 414 VAL B 417 1 O GLY B 414 N PHE B 355
SHEET 5 E 6 ARG B 440 ALA B 445 1 O ARG B 440 N ILE B 415
SHEET 6 E 6 PHE B 461 SER B 464 1 O VAL B 463 N ALA B 445
SHEET 1 F 4 ALA B 490 PRO B 495 0
SHEET 2 F 4 ARG B 544 GLY B 549 -1 O LEU B 547 N PHE B 492
SHEET 3 F 4 SER B 517 GLU B 522 -1 N ALA B 520 O ILE B 546
SHEET 4 F 4 ILE B 529 ILE B 531 -1 O LEU B 530 N ILE B 521
SHEET 1 G 6 LYS C 176 TYR C 179 0
SHEET 2 G 6 PHE C 156 THR C 160 1 N VAL C 158 O VAL C 178
SHEET 3 G 6 ILE C 133 PHE C 136 1 N ILE C 135 O VAL C 157
SHEET 4 G 6 SER C 198 ALA C 201 1 O ILE C 200 N LEU C 134
SHEET 5 G 6 ILE C 223 VAL C 226 1 O ILE C 224 N ALA C 201
SHEET 6 G 6 GLN C 243 VAL C 245 1 O GLN C 243 N ALA C 225
SHEET 1 H 5 ALA C 266 LEU C 269 0
SHEET 2 H 5 GLN C 276 PRO C 281 -1 O ILE C 277 N ILE C 268
SHEET 3 H 5 LEU C 328 GLY C 333 -1 O LEU C 331 N ALA C 278
SHEET 4 H 5 SER C 304 GLU C 310 -1 N SER C 304 O ALA C 332
SHEET 5 H 5 SER C 313 THR C 315 -1 O THR C 315 N VAL C 308
SHEET 1 I 6 VAL C 393 TYR C 395 0
SHEET 2 I 6 PHE C 377 ASP C 381 1 N LEU C 379 O VAL C 394
SHEET 3 I 6 ILE C 354 ILE C 357 1 N ILE C 356 O ILE C 378
SHEET 4 I 6 GLY C 414 VAL C 417 1 O ILE C 416 N PHE C 355
SHEET 5 I 6 ARG C 440 ALA C 445 1 O VAL C 442 N ILE C 415
SHEET 6 I 6 PHE C 461 SER C 464 1 O VAL C 463 N ALA C 443
SHEET 1 J 4 MET C 489 PRO C 495 0
SHEET 2 J 4 ARG C 544 THR C 550 -1 O LEU C 545 N ARG C 494
SHEET 3 J 4 SER C 517 GLU C 522 -1 N GLU C 522 O ARG C 544
SHEET 4 J 4 LEU C 530 ILE C 531 -1 O LEU C 530 N ILE C 521
SHEET 1 K 6 LYS D 176 TYR D 179 0
SHEET 2 K 6 LEU D 155 THR D 160 1 N VAL D 158 O VAL D 178
SHEET 3 K 6 HIS D 132 PHE D 136 1 N ILE D 135 O VAL D 157
SHEET 4 K 6 SER D 198 ALA D 201 1 O ILE D 200 N LEU D 134
SHEET 5 K 6 ILE D 223 VAL D 226 1 O ILE D 224 N ILE D 199
SHEET 6 K 6 GLN D 243 VAL D 245 1 O VAL D 245 N ALA D 225
SHEET 1 L 6 VAL D 393 TYR D 395 0
SHEET 2 L 6 PHE D 377 ASP D 381 1 N LEU D 379 O VAL D 394
SHEET 3 L 6 ILE D 354 ILE D 357 1 N ILE D 356 O ILE D 378
SHEET 4 L 6 GLY D 414 VAL D 417 1 O ILE D 416 N PHE D 355
SHEET 5 L 6 ARG D 440 ALA D 445 1 O ARG D 440 N ILE D 415
SHEET 6 L 6 PHE D 461 SER D 464 1 O VAL D 463 N ALA D 445
LINK O THR A 68 K K A 602 1555 1555 2.90
LINK O LEU A 69 K K A 601 1555 1555 2.73
LINK O LEU A 69 K K A 602 1555 1555 2.48
LINK O GLY A 70 K K A 601 1555 1555 3.10
LINK O GLY A 70 K K B 601 1555 1555 2.96
LINK O PHE A 71 K K B 601 1555 1555 3.08
LINK NE2 HIS A 359 ZN ZN A 604 1555 1555 2.42
LINK SG CYS A 364 ZN ZN A 604 1555 1555 2.58
LINK SG CYS A 388 ZN ZN A 604 1555 1555 2.65
LINK ND1 HIS A 391 ZN ZN A 604 1555 1555 2.49
LINK O GLU A 449 CA CA A 605 1555 1555 3.03
LINK OD1 ASN A 450 CA CA A 605 1555 1555 3.05
LINK OE1 GLN A 453 CA CA A 605 1555 1555 3.01
LINK K K A 601 O LEU B 69 1555 1555 2.68
LINK K K A 601 O GLY B 70 1555 1555 3.02
LINK K K A 602 O THR B 68 1555 1555 2.94
LINK K K A 602 O LEU B 69 1555 1555 2.84
LINK CA CA A 605 O THR B 183 1555 1555 2.94
LINK CA CA A 605 OD1 ASN B 210 1555 1555 3.05
LINK CA CA A 605 OG1 THR B 214 1555 1555 3.15
LINK O GLY B 70 K K B 601 1555 1555 2.96
LINK O PHE B 71 K K B 601 1555 1555 2.80
LINK NE2 HIS B 359 ZN ZN B 604 1555 1555 2.55
LINK SG CYS B 364 ZN ZN B 604 1555 1555 2.72
LINK SG CYS B 388 ZN ZN B 604 1555 1555 2.68
LINK ND1 HIS B 391 ZN ZN B 604 1555 1555 2.44
LINK O GLU B 449 CA CA B 605 1555 1555 2.88
LINK OE1 GLN B 453 CA CA B 605 1555 1555 3.14
LINK O THR C 68 K K C 601 1555 1555 2.83
LINK O LEU C 69 K K C 601 1555 1555 3.46
LINK O LEU C 69 K K C 602 1555 1555 3.04
LINK O GLY C 70 K K C 602 1555 1555 3.08
LINK O GLY C 70 K K C 603 1555 1555 2.98
LINK O PHE C 71 K K C 603 1555 1555 3.35
LINK O THR C 183 CA CA C 605 1555 1555 2.98
LINK OD1 ASN C 210 CA CA C 605 1555 1555 2.92
LINK OG1 THR C 214 CA CA C 605 1555 1555 3.06
LINK NE2 HIS C 359 ZN ZN C 604 1555 1555 2.52
LINK SG CYS C 364 ZN ZN C 604 1555 1555 2.61
LINK SG CYS C 388 ZN ZN C 604 1555 1555 2.63
LINK ND1 HIS C 391 ZN ZN C 604 1555 1555 2.42
LINK O GLU C 449 CA CA C 606 1555 1555 3.01
LINK OD1 ASN C 450 CA CA C 606 1555 1555 3.18
LINK OE1 GLN C 453 CA CA C 606 1555 1555 3.16
LINK K K C 601 O THR D 68 1555 1555 2.51
LINK K K C 601 O LEU D 69 1555 1555 3.14
LINK K K C 602 O LEU D 69 1555 1555 2.62
LINK K K C 602 O GLY D 70 1555 1555 2.90
LINK K K C 603 O GLY D 70 1555 1555 2.81
LINK K K C 603 O PHE D 71 1555 1555 3.30
LINK CA CA C 606 O THR D 183 1555 1555 3.03
LINK CA CA C 606 OD1 ASN D 210 1555 1555 2.94
LINK CA CA C 606 OG1 THR D 214 1555 1555 3.02
LINK NE2 HIS D 359 ZN ZN D 603 1555 1555 2.43
LINK SG CYS D 364 ZN ZN D 603 1555 1555 2.61
LINK SG CYS D 388 ZN ZN D 603 1555 1555 2.65
CISPEP 1 LYS A 373 PRO A 374 0 -5.46
CISPEP 2 ILE B 345 GLY B 346 0 -2.21
CISPEP 3 LYS B 373 PRO B 374 0 -5.05
CRYST1 234.323 111.442 164.743 90.00 134.93 90.00 C 1 2 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004268 0.000000 0.004258 0.00000
SCALE2 0.000000 0.008973 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008575 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
